Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21243 (PSA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-1

EC=3.4.25.1
Alternative name(s):
Macropain subunit C7-alpha
Multicatalytic endopeptidase complex C7
Proteasome component C7-alpha
Proteasome component Y8
Proteinase YSCE subunit 7
SCL1 suppressor protein
Gene names
Name:SCL1
Synonyms:PRC2, PRS2
Ordered Locus Names:YGL011C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1. Ref.7

Subcellular location

Cytoplasm. Nucleus Ref.8.

Miscellaneous

Present with 15200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence caution

The sequence AAA35020.1 differs from that shown. Reason: Frameshift at position 26.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRE10P212426EBI-13975,EBI-13963
PRE8P236396EBI-13975,EBI-13959

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 252251Proteasome subunit alpha type-1
PRO_0000124141

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue2371Phosphoserine Ref.10

Secondary structure

.................................................. 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21243 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 5B938C862BC8D7EB

FASTA25228,001
        10         20         30         40         50         60 
MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC TVVISQKKVP 

        70         80         90        100        110        120 
DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE AAEFRYKYGY DMPCDVLAKR 

       130        140        150        160        170        180 
MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL GPSIYKTDPA GYYVGYKATA TGPKQQEITT 

       190        200        210        220        230        240 
NLENHFKKSK IDHINEESWE KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN 

       250 
IEERLVAIAE QD 

« Hide

References

« Hide 'large scale' references
[1]"The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growth."
Balzi E., Chen W., Capieaux E., McCusker J.H., Haber J.E., Goffeau A.
Gene 83:271-279(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
J. Biol. Chem. 265:16604-16613(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187 AND 189-198.
[3]"Molecular cloning and functional analysis of three subunits of yeast proteasome."
Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 26786 / X2180-1A.
[4]"The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance."
Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.
Yeast 7:287-299(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46191 / IL125-2B.
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIC1.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Structure of 20S proteasome from yeast at 2.4-A resolution."
Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[14]"Structural basis for the activation of 20S proteasomes by 11S regulators."
Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
[15]"A gated channel into the proteasome core particle."
Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D.
Nat. Struct. Biol. 7:1062-1067(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[16]"Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
Groll M., Koguchi Y., Huber R., Kohno J.
J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[17]"TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[18]"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
Groll M., Huber R., Potts B.C.M.
J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[19]"Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[20]"Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 IN COMPLEX WITH THE PROTEASOME.
[21]"Near-atomic resolution structural model of the yeast 26S proteasome."
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31430 Genomic DNA. Translation: AAA35020.1. Frameshift.
X56971 Genomic DNA. Translation: CAA40292.1.
M55440 mRNA. Translation: AAA35228.1.
M63641 Genomic DNA. Translation: AAA34909.1.
X56732 Genomic DNA. Translation: CAA40056.1.
S58126 Genomic DNA. Translation: AAD13894.1.
Z72533 Genomic DNA. Translation: CAA96711.1.
BK006941 Genomic DNA. Translation: DAA08087.1.
PIRSNBYS1. S11199.
RefSeqNP_011504.3. NM_001180876.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20A/O1-252[»]
1G0UX-ray2.40G/U1-252[»]
1G65X-ray2.25G/U10-252[»]
1JD2X-ray3.002/G10-252[»]
1RYPX-ray1.90A/O10-252[»]
1VSYX-ray3.00A/O10-252[»]
1Z7QX-ray3.22A/O1-252[»]
2F16X-ray2.80G/U10-252[»]
2FAKX-ray2.80G/U10-252[»]
2GPLX-ray2.81G/U10-252[»]
2ZCYX-ray2.90G/U1-252[»]
3BDMX-ray2.70G/U1-252[»]
3D29X-ray2.60G/U12-252[»]
3DY3X-ray2.81G/U10-252[»]
3DY4X-ray2.80G/U10-252[»]
3E47X-ray3.00G/U10-252[»]
3GPJX-ray2.70G/U10-252[»]
3GPTX-ray2.41G/U10-252[»]
3GPWX-ray2.50G/U10-252[»]
3HYEX-ray2.50G/U10-252[»]
3L5QX-ray3.00A/C10-252[»]
3MG0X-ray2.68G/U10-252[»]
3MG4X-ray3.11G/U10-252[»]
3MG6X-ray2.60G/U1-252[»]
3MG7X-ray2.78G/U1-252[»]
3MG8X-ray2.59G/U1-252[»]
3NZJX-ray2.40G/U1-252[»]
3NZWX-ray2.50G/U1-252[»]
3NZXX-ray2.70G/U1-252[»]
3OEUX-ray2.60G/U10-252[»]
3OEVX-ray2.85G/U10-252[»]
3OKJX-ray2.70G/U10-252[»]
3SDIX-ray2.65G/U10-252[»]
3SDKX-ray2.70G/U10-252[»]
3SHJX-ray2.80G/U10-252[»]
3TDDX-ray2.70G/U10-252[»]
3UN4X-ray3.40G/U1-252[»]
3UN8X-ray2.70G/U1-252[»]
4B4Telectron microscopy7.40A1-252[»]
4C0Velectron microscopy9.80A1-252[»]
4EU2X-ray2.51A/O10-250[»]
4FZCX-ray2.80G/U10-252[»]
4FZGX-ray3.00G/U10-252[»]
4G4SX-ray2.49A1-252[»]
4GK7X-ray2.80G/U10-252[»]
4HNPX-ray2.80G/U10-252[»]
4HRCX-ray2.80G/U10-252[»]
4HRDX-ray2.80G/U10-252[»]
4INRX-ray2.70G/U1-252[»]
4INTX-ray2.90G/U1-252[»]
4INUX-ray3.10G/U1-252[»]
4J70X-ray2.80G/U1-252[»]
4JSQX-ray2.80G/U1-252[»]
4JSUX-ray2.90G/U1-252[»]
4JT0X-ray3.10G/U1-252[»]
4LQIX-ray2.70G/U10-252[»]
4NNNX-ray2.50G/U1-252[»]
4NNWX-ray2.60G/U1-252[»]
4NO1X-ray2.50G/U1-252[»]
4NO6X-ray3.00G/U1-252[»]
4NO8X-ray2.70G/U1-252[»]
4NO9X-ray2.90G/U1-252[»]
ProteinModelPortalP21243.
SMRP21243. Positions 10-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33235. 74 interactions.
DIPDIP-2810N.
IntActP21243. 28 interactions.
MINTMINT-525412.

Protein family/group databases

MEROPST01.971.

2D gel databases

UCD-2DPAGEP21243.

Proteomic databases

PaxDbP21243.
PeptideAtlasP21243.
PRIDEP21243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL011C; YGL011C; YGL011C.
GeneID852873.
KEGGsce:YGL011C.

Organism-specific databases

CYGDYGL011c.
SGDS000002979. SCL1.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074807.
HOGENOMHOG000091084.
KOK02730.
OMAMSRTSYD.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-30533-MONOMER.

Gene expression databases

GenevestigatorP21243.

Family and domain databases

InterProIPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21243.
NextBio972505.
PROP21243.

Entry information

Entry namePSA1_YEAST
AccessionPrimary (citable) accession number: P21243
Secondary accession number(s): D6VUC6, P15708
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references